Research workbench
Crystal structure of H-nox protein from nostoc sp V52W/L67W double- mutant.
Analyse Crystal structure of H-nox protein from nostoc sp V52W/L67W double- mutant. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DXI
- Type
- protein
- Length
- 189 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- H-nox
- UniProt
- A0A1Z4KG06
- Ligands
- HEM
- Pockets
- 1 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | H-nox | protein | 189 | 52% helix, 16% strand | A0A1Z4KG06 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 354 | 0.85 | 0.93 | 38 | HEM |
Compared structures
- 6DXI · Crystal structure of H-NOX protein from Nostoc sp V52W/L67W double-mutant. · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A1Z4KG06
- Elsewhere: RCSB PDB 6DXI · PDBe 6DXI · UniProt A0A1Z4KG06
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